Opat A S, van Vliet C, Gleeson P A
Department of Pathology and Immunology, Monash University Medical School, Melbourne, Commercial Road, Melbourne, Victoria 3181, Australia.
Biochimie. 2001 Aug;83(8):763-73. doi: 10.1016/s0300-9084(01)01312-8.
The localisation of glycosylation enzymes within the Golgi apparatus is fundamental to the regulation of glycoprotein and glycolipid biosynthesis. Regions responsible for specifying Golgi localisation have been identified in numerous Golgi resident enzymes. The transmembrane domain of Golgi glycosyltransferases provides a dominant localisation signal and in many cases there are also major contributions from the lumenal domain. The mechanism by which these targeting domains function in maintaining an asymmetric distribution of Golgi resident glycosylation enzymes has been intensely debated in recent years. It is now clear that the targeting of Golgi resident enzymes is intimately associated with the organisation of Golgi membranes and the control of protein and lipid traffic in both anterograde and retrograde directions. Here we discuss the recent advances into how Golgi targeting signals of glycosylation enzymes function, and propose a model for maintaining the steady-state localisation of Golgi glycosyltransferases.
糖基化酶在高尔基体中的定位对于糖蛋白和糖脂生物合成的调控至关重要。在众多高尔基体驻留酶中已鉴定出负责指定高尔基体定位的区域。高尔基体糖基转移酶的跨膜结构域提供了主要的定位信号，并且在许多情况下，腔结构域也有重要作用。近年来，这些靶向结构域在维持高尔基体驻留糖基化酶不对称分布中发挥作用的机制一直存在激烈争论。现在很清楚，高尔基体驻留酶的靶向与高尔基体膜的组织以及蛋白质和脂质在顺行和逆行方向上的运输控制密切相关。在此，我们讨论糖基化酶的高尔基体靶向信号如何发挥作用的最新进展，并提出一个维持高尔基体糖基转移酶稳态定位的模型。
